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Snake venom C-type lectins as tools in platelet research.
K J Clemetson1, J Polgár, J M Clemetson
1Theodor Kocher Institute, University of Berne, Switzerland. clemetson@tki.unibe.ch
Platelets
|June 24, 2006
Summary
Snake C-type lectins, found in venom, interact with platelet receptors to modulate blood clotting. Their unique structure and function offer insights into platelet activation and inhibition for research applications.
Area of Science:
- Biochemistry
- Toxicology
- Hematology
Background:
- Snake venoms contain C-type lectins, a protein group structurally similar to classic C-type lectins.
- These venom lectins possess unique structural modifications, including a truncated loop for calcium/sugar binding and disulfide-linked heterodimers.
Purpose of the Study:
- To explore the structure-function relationship of snake C-type lectins.
- To investigate the role of these lectins in modulating platelet activity.
- To highlight their utility as research tools for studying platelet function.
Main Methods:
- Structural analysis of snake C-type lectins.
- Biochemical assays to assess interactions with platelet receptors.
- Functional assays to determine effects on platelet activation and inhibition.
Main Results:
- Snake C-type lectins exhibit structural adaptations distinct from classic lectins.
- These proteins effectively interact with platelet receptors, influencing platelet activation.
- Specific examples demonstrate the application of these lectins in platelet research.
Conclusions:
- Snake C-type lectins are versatile proteins with significant roles in venom and platelet biology.
- Their unique structural features enable potent modulation of platelet function.
- These venom-derived lectins serve as valuable tools for advancing the understanding of platelet physiology.

